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Koji Muramoto

Researcher at Tohoku University

Publications -  212
Citations -  7687

Koji Muramoto is an academic researcher from Tohoku University. The author has contributed to research in topics: Lectin & Peptide sequence. The author has an hindex of 45, co-authored 212 publications receiving 7185 citations. Previous affiliations of Koji Muramoto include Tokyo University of Agriculture & Kitasato University.

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Antioxidant Activity of Designed Peptides Based on the Antioxidative Peptide Isolated from Digests of a Soybean Protein

TL;DR: Antioxidative peptides showed synergistic effects with nonpeptidic antioxidants as observed in soybean protein and, among the peptides tested, Pro-His-His was the most antioxidative.
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Antioxidative Properties of Histidine-Containing Peptides Designed from Peptide Fragments Found in the Digests of a Soybean Protein

TL;DR: Although the histidine-containing peptides had a quenching activity on singlet oxygen, they did not show antioxidative activity in an 2,2'-azobis(2,4-dimethylvaleronitrile)-induced oxidation system or scavenging effects on 1,1-diphenyl-2-picrylhydrazyl radical and superoxide.
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Structural Analysis of Antioxidative Peptides from Soybean .beta.-Conglycinin

TL;DR: Protease hydrolyses of a soybean protein, beta-conglycinin (7S protein), yielded antioxidative activity against the peroxidation of linoleic acid in an aqueous system at pH 7.0.
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Antioxidative properties of tripeptide libraries prepared by the combinatorial chemistry.

TL;DR: The present results allow us to understand why protein digests have such a variety of antioxidative properties, including strong radical scavenging activities, but very weak peroxynitrite scavenging activity.
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Angiotensin I-Converting Enzyme Inhibitory Peptides Derived from Wakame (Undaria pinnatifida) and Their Antihypertensive Effect in Spontaneously Hypertensive Rats

TL;DR: The present study showed that antihypertensive effect in the hydrolysates of wakame by Protease S "Amano" was attributed to these peptides, which have resistance against gastrointestinal proteases in vitro.